UniProt Accession

 PRDX3_MOUSE; P20108 

Genbank Protein ID

 M28723; AF211938; AF211933; AF211934; AF211935; AF211936; AF211937; AK002448; BC005626 

Genbank Nucleotide ID

 AAA39524.1; AAF63705.1; AAF63705.1; AAF63705.1; AAF63705.1; AAF63705.1; AAF63705.1; BAB22108.1; AAH05626.1 

Protein Name

 Thioredoxin-dependent peroxide reductase, mitochondrial 

Protein Synonyms/Alias

 Antioxidant protein 1; AOP-1; PRX III; Perioredoxin-3; Protein MER5 

Gene Name

 Prdx3 

Gene Synonyms/Alias

 Aop1; Mer5 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
74	TQHAPYFKGTAVVNG	acetylation	[1]
84	AVVNGEFKELSLDDF	acetylation	[2, 3, 4]
84	AVVNGEFKELSLDDF	succinylation	[3]
92	ELSLDDFKGKYLVLF	acetylation	[1, 2, 3, 4, 5, 6, 7, 8]
92	ELSLDDFKGKYLVLF	succinylation	[3]
92	ELSLDDFKGKYLVLF	ubiquitination	[9]
150	AWINTPRKNGGLGHM	acetylation	[1]
242	TPESPTIKPSPTASK	acetylation	[4, 7]
249	KPSPTASKEYFEKVH	acetylation	[1]
254	ASKEYFEKVHQ****	acetylation	[1, 2, 3]
254	ASKEYFEKVHQ****	succinylation	[3]
254	ASKEYFEKVHQ****	ubiquitination	[9]

Reference

 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

Functional Description

 Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical- generating system. 

Sequence Annotation

 DOMAIN 64 222 Thioredoxin.
 ACT_SITE 109 109 Cysteine sulfenic acid (-SOH)
 MOD_RES 92 92 N6-acetyllysine (By similarity).
 DISULFID 109 109 Interchain (with C-230); in linked form
 DISULFID 230 230 Interchain (with C-109); in linked form  

Keyword

 Acetylation; Antioxidant; Complete proteome; Direct protein sequencing; Disulfide bond; Mitochondrion; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 257 AA 

Protein Sequence

Gene Ontology

 GO:0005769; C:early endosome; IEA:Compara.
 GO:0008385; C:IkappaB kinase complex; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Compara.
 GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
 GO:0051920; F:peroxiredoxin activity; IEA:EC.
 GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
 GO:0001893; P:maternal placenta development; IMP:MGI.
 GO:0007005; P:mitochondrion organization; IEA:Compara.
 GO:0030099; P:myeloid cell differentiation; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0033673; P:negative regulation of kinase activity; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Compara.
 GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IMP:MGI. 

Interpro

 IPR000866; AhpC/TSA.
 IPR024706; Peroxiredoxin_AhpC-typ.
 IPR019479; Peroxiredoxin_C.
 IPR012336; Thioredoxin-like_fold. 

Pfam

 PF10417; 1-cysPrx_C
 PF00578; AhpC-TSA 

SMART

  

PROSITE

 PS51352; THIOREDOXIN_2 

PRINTS